Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005179 | molecular_function | hormone activity |
A | 0005576 | cellular_component | extracellular region |
B | 0005179 | molecular_function | hormone activity |
B | 0005576 | cellular_component | extracellular region |
C | 0005179 | molecular_function | hormone activity |
C | 0005576 | cellular_component | extracellular region |
D | 0005179 | molecular_function | hormone activity |
D | 0005576 | cellular_component | extracellular region |
E | 0005179 | molecular_function | hormone activity |
E | 0005576 | cellular_component | extracellular region |
F | 0005179 | molecular_function | hormone activity |
F | 0005576 | cellular_component | extracellular region |
G | 0005179 | molecular_function | hormone activity |
G | 0005576 | cellular_component | extracellular region |
H | 0005179 | molecular_function | hormone activity |
H | 0005576 | cellular_component | extracellular region |
I | 0005179 | molecular_function | hormone activity |
I | 0005576 | cellular_component | extracellular region |
J | 0005179 | molecular_function | hormone activity |
J | 0005576 | cellular_component | extracellular region |
K | 0005179 | molecular_function | hormone activity |
K | 0005576 | cellular_component | extracellular region |
L | 0005179 | molecular_function | hormone activity |
L | 0005576 | cellular_component | extracellular region |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE IPH A 22 |
Chain | Residue |
B | LEU11 |
B | ALA14 |
H | LEU17 |
A | CYS6 |
A | ILE10 |
A | CYS11 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE IPH C 22 |
Chain | Residue |
C | CYS6 |
C | ILE10 |
C | CYS11 |
D | LEU11 |
D | ALA14 |
J | LEU17 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE IPH E 22 |
Chain | Residue |
E | CYS6 |
E | ILE10 |
E | CYS11 |
F | LEU11 |
F | ALA14 |
L | LEU17 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE IPH G 22 |
Chain | Residue |
B | LEU17 |
G | CYS6 |
G | ILE10 |
G | CYS11 |
H | LEU11 |
H | ALA14 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE IPH I 22 |
Chain | Residue |
D | LEU17 |
I | CYS6 |
I | ILE10 |
I | CYS11 |
J | LEU11 |
J | ALA14 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE IPH K 22 |
Chain | Residue |
F | LEU17 |
K | CYS6 |
K | ILE10 |
K | CYS11 |
L | LEU11 |
L | ALA14 |
site_id | ZN1 |
Number of Residues | 3 |
Details | IN THE CRYSTAL STRUCTURE, 1ZNJ, THESE RESIDUES ARE COORDINATED BY A ZINC ATOM. THE ZINC ATOM IS NOT INCLUDED SINCE IT COULD NOT BE OBSERVED IN THE NMR SPECTRA. |
Chain | Residue |
B | HIS10 |
F | HIS10 |
J | HIS10 |
site_id | ZN2 |
Number of Residues | 3 |
Details | IN THE CRYSTAL STRUCTURE, 1ZNJ, THESE RESIDUES ARE COORDINATED BY A ZINC ATOM. THE ZINC ATOM IS NOT INCLUDED SINCE IT COULD NOT BE OBSERVED IN THE NMR SPECTRA. |
Chain | Residue |
D | HIS10 |
H | HIS10 |
L | HIS10 |
Functional Information from PROSITE/UniProt
site_id | PS00262 |
Number of Residues | 15 |
Details | INSULIN Insulin family signature. CCTSiCSlyqLenyC |
Chain | Residue | Details |
A | CYS6-CYS20 | |